The biological function of cells, and ultimately of tissues, organs and body, depends on the correct folding of a network of thousands of proteins. The amino acid sequence of a given protein contains the required information to fold it into a functional, specific three-dimensional structure. In healthy cells, proteins fold properly into their native conformation and, if they do not, the misfolding should be corrected by chaperone proteins (Bukau B, Weissman J, Horwich A. Cell. 2006; 125(3):443-51). In protein misfolding disorders (PMDs) or conformational disorders (CDs), however, misfolding of a protein results in its degradation (e.g. cystic fibrosis) or in its aggregation and accumulation as protein deposits near the site of its cellular production or in diverse tissues (Soto C, Estrada L D. Arch Neurol. 2008; 65(2):184-9; Winklhofer K F, Tatzelt J, Haass C. EMBO J. 2008; 27(2):336-49; Gregersen N. J Inherit Metab Dis. 2006; 29(2-3):456-70).
In the figures, where used, the expression “w.o” indicates “without”.